Identification
Name:Superoxide dismutase [Mn]
Synonyms:
  • MnSOD
Gene Name:sodA
Enzyme Class:
Biological Properties
General Function:Involved in superoxide dismutase activity
Specific Function:Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:Not Available
KEGG Reactions:
2.0Thumb+2.0Thumb1.0Thumb+1.0Thumb
EcoCyc Reactions:
2.0Thumb+2.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB23001superoxideMetaboCard
ECMDB21285Superoxide anionMetaboCard
GO Classification:
Function
antioxidant activity
binding
cation binding
ion binding
metal ion binding
superoxide dismutase activity
Process
cellular metabolic process
metabolic process
oxidation reduction
oxygen and reactive oxygen species metabolic process
superoxide metabolic process
Gene Properties
Blattner:b3908
Gene OrientationClockwise
Centisome Percentage:88.34
Left Sequence End4098833
Right Sequence End4099453
Gene Sequence:
>621 bp
ATGAGCCAGTTTTTTTATATTCATCCTGATAACCCACAGCAACGTCTGATCAACCAGGCG
GTGGAGATCGTGCGTAAAGGCGGGGTGATTGTTTATCCAACTGATTCCGGCTATGCGCTC
GGCTGTAAAATTGAAGATAAAAACGCGATGGAGCGTATTTGTCGTATTCGCCAGCTGCCG
GACGGTCACAACTTTACCCTGATGTGTCGCGATCTTTCTGAACTCTCGACCTATTCATTT
GTTGATAACGTTGCGTTTCGTTTAATGAAAAACAACACGCCGGGCAACTATACCTTCATC
CTGAAGGGGACGAAGGAAGTGCCACGCCGTCTGTTGCAGGAAAAACGCAAAACCATCGGT
ATGCGTGTGCCTTCTAACCCTATCGCTCAGGCGTTACTTGAAGCATTGGGCGAACCGATG
CTTTCCACTTCGCTAATGCTGCCAGGCAGCGAATTTACCGAATCGGACCCGGAAGAAATT
AAAGATCGTCTGGAAAAACAGGTAGATTTGATTATTCACGGCGGCTATCTCGGGCAGAAA
CCGACAACGGTTATTGATCTTACCGATGATACGCCGGTCGTGGTGCGTGAAGGCGTAGGT
GATGTGAAGCCTTTCTTATAA
Protein Properties
Pfam Domain Function:
Protein Residues:206
Protein Molecular Weight:23097
Protein Theoretical pI:7
PDB File:1D5N
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Superoxide dismutase [Mn]
MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITK
LDQLPADKKTVLRNNAGGHANHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKA
AASRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGASGFPIMGLDVWEHAYYLKFQN
RRPDYIKEFWNVVNWDEAAARFAAKK
References
External Links:
ResourceLink
Uniprot ID:P00448
Uniprot Name:SODM_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674890
PDB ID:1D5N
Ecogene ID:EG10953
Ecocyc:EG10953
ColiBase:b3908
Kegg Gene:b3908
EchoBASE ID:EB0946
CCDB:SODM_ECOLI
BacMap:49176442
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Borgstahl, G. E., Pokross, M., Chehab, R., Sekher, A., Snell, E. H. (2000). "Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase." J Mol Biol 296:951-959. Pubmed: 10686094
  • Edwards, R. A., Whittaker, M. M., Whittaker, J. W., Baker, E. N., Jameson, G. B. (2001). "Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase." Biochemistry 40:15-27. Pubmed: 11141052
  • Edwards, R. A., Whittaker, M. M., Whittaker, J. W., Baker, E. N., Jameson, G. B. (2001). "Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity." Biochemistry 40:4622-4632. Pubmed: 11294629
  • Garcia-Martin, C., Baldoma, L., Badia, J., Aguilar, J. (1992). "Nucleotide sequence of the rhaR-sodA interval specifying rhaT in Escherichia coli." J Gen Microbiol 138:1109-1116. Pubmed: 1339463
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
  • Renault, J. P., Verchere-Beaur, C., Morgenstern-Badarau, I., Piccioli, M. (1997). "Paramagnetic NMR spectroscopy of native and cobalt substituted manganese superoxide dismutase from Escherichia coli." FEBS Lett 401:15-19. Pubmed: 9003797
  • Steinman, H. M. (1978). "The amino acid sequence of mangano superoxide dismutase from Escherichia coli B." J Biol Chem 253:8708-8720. Pubmed: 363708
  • Takeda, Y., Avila, H. (1986). "Structure and gene expression of the E. coli Mn-superoxide dismutase gene." Nucleic Acids Res 14:4577-4589. Pubmed: 3520487
  • Tate, C. G., Muiry, J. A., Henderson, P. J. (1992). "Mapping, cloning, expression, and sequencing of the rhaT gene, which encodes a novel L-rhamnose-H+ transport protein in Salmonella typhimurium and Escherichia coli." J Biol Chem 267:6923-6932. Pubmed: 1551902
  • Touati, D. (1988). "Transcriptional and posttranscriptional regulation of manganese superoxide dismutase biosynthesis in Escherichia coli, studied with operon and protein fusions." J Bacteriol 170:2511-2520. Pubmed: 3131302